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#secondary active transport

8 public questions tagged with this topic.

Membrane Transportation

What is the primary function of Na+/K+ ATPase in maintaining secondary active transport?

Primary role of Na+/K+ ATPase in context of secondary active transport is generation and maintenance of electrochemical sodium gradient that powers numerous symporters and antiporters. By pumping three Na+ outward and two K+ inward per ATP hydrolyzed, it creates chemical gradient low intracellular Na+ and electrical gradient interior negative near minus 70 mV. Combined sodium motive force represents stored free energy. Solute carrier families SLC5 SGLT, SLC6 neurotransmitter transporters, SLC38 amino acid transporters, SLC9 NHE and SLC8 NCX exploit this force allowing Na+ to move downhill whil

Ref: Alberts et al., 7th ed., Chapter 11, Na+/K+ pump and secondary transport coupling.

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Membrane Transportation

In secondary active transport, lactose permease in E. coli utilizes:

Secondary active lactose permease LacY does not itself hydrolyze ATP nor perform direct phosphorylation of sugar substrate like phosphotransferase systems that import glucose as glucose-6-phosphate. Instead energy source is electrochemical proton gradient across E. coli inner membrane established by respiratory chain proton pumping. Lactose entry is strictly coupled to downhill H+ flow: one proton symported per lactose disaccharide. Experimental evidence shows that abolishing proton motive force with uncouplers carbonyl cyanide m-chlorophenyl hydrazone, nigericin, or by inhibiting respiration

Ref: Kaback et al., J Gen Physiol 2008, Proton coupling LacY; Poolman et al., Mol Microbiol 2004.

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Membrane Transportation

Which of the following is not a characteristic of secondary active transport?

Secondary active transport refers to movement of solute against its concentration gradient energized indirectly by ion electrochemical gradient established by primary active pumps, not by direct ATP binding and hydrolysis at transport protein itself. Hallmarks include dependence on Na+/K+ ATPase or H+-ATPase to maintain Na+ or H+ motive force, inhibition by collapse of gradient with ionophores or ouabain, and involvement of symport or antiport mechanisms where downhill flow of driving ion drags substrate uphill. Protein operates by alternating access rocker-switch mechanism without Walker A AT

Ref: Alberts et al., 7th ed., Chapter 11, Distinction primary vs secondary active transport.

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Membrane Transportation

The mechanism of proton-coupled lactose transport in E. coli is an example of:

In Escherichia coli, lactose accumulation during lactose operon induction exemplifies secondary active transport powered by proton motive force, not direct ATP hydrolysis or simple diffusion. LacY permease co-transports one H+ and one lactose molecule; downhill H+ movement through transporter allows uphill lactose concentration. Gradient is sustained by primary H+ extrusion by respiratory chain complexes pumping protons outward, generating proton electrochemical gradient consisting of pH and membrane potential. When respiration is active, periplasmic proton binds outward-open LacY, increases a

Ref: Kaback, Biochim Biophys Acta 2015, LacY proton coupling; Alberts, Chapter 11 secondary transport.

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Membrane Transportation

Which of the following describes Na+/amino acid symporters?

Sodium-amino acid symporters belong to SLC6, SLC1 and SLC38 families mediating concentrative uptake of neutral, acidic and basic amino acids in intestinal epithelium, kidney proximal tubule, neurons and astrocytes. They co-transport one to two Na+ ions with one amino acid molecule, using sodium electrochemical gradient generated by Na+/K+ ATPase to drive amino acid accumulation against gradient up to hundred-fold, essential for protein synthesis, neurotransmitter precursor supply, osmolyte production and mTOR signaling. Transport cycle involves alternating access where Na+ binding increases af

Ref: Broer, Physiol Rev 2008, Amino acid transporters; Alberts et al., Chapter 11 nutrient symport.

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Membrane Transportation

What is the driving force for Na+-Glucose Symporters (SGLT1)?

Sodium-glucose symporters accumulate glucose far above extracellular concentration without directly hydrolyzing ATP. Driving force is electrochemical sodium gradient composed of chemical component low intracellular Na+ plus electrical component interior negative membrane potential, together producing steep inward Na+ motive force. Basolateral Na+/K+ ATPase primary active pump continuously extrudes three Na+ and imports two K+ per ATP, keeping cytosolic Na+ around 12 mM versus lumen 140 mM. SGLT1 exploits this stored energy by allowing Na+ to flow downhill through transporter coupled stoichiome

Ref: Alberts et al., 7th ed., Chapter 11, Na+-driven glucose symport energetics; Wright 2013.

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Membrane Transportation

Which type of transport does SGLT1 use?

SGLT1, SLC5A1, is apical sodium-glucose cotransporter highly expressed in brush border of small intestinal enterocytes and S3 segment of kidney proximal tubule. It operates as secondary active transporter, not primary ATPase nor simple facilitator. Stoichiometry of two Na+ to one glucose allows accumulation of glucose against its concentration gradient using electrochemical sodium gradient established by basolateral Na+/K+ ATPase that maintains low intracellular Na+. Transport follows alternating access mechanism: outward-open binds Na+ increasing glucose affinity, sugar binding triggers outwa

Ref: Wright et al., Physiol Rev 2011, Sodium-glucose cotransporters SLC5 family.

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Membrane Transportation

The Na+/glucose transporter (SGLT1) is an example of:

Sodium-dependent glucose transport exemplifies secondary active symport coupling uphill absorption to downhill sodium entry. SGLT1 gene SLC5A1 located apically in intestinal villus enterocytes and kidney proximal tubule contains fourteen transmembrane helices in LeuT fold forming cavity with two sodium sites Na1 and Na2 plus glucose pocket recognizing hydroxyls. Cycle has ordered binding: two sodium ions bind first increasing affinity for D-glucose by opening outer gate then protein transitions from outward open to occluded to inward open releasing cargo inside. Both substrates move same direc

Ref: Wright et al., Journal of Biological Chemistry 2004: SGLT1 as Sodium Glucose Symport.

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